1O3S

PROTEIN-DNA RECOGNITION AND DNA DEFORMATION REVEALED IN CRYSTAL STRUCTURES OF CAP-DNA COMPLEXES

Replaces:  1DB9

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X25
Synchrotron site	NSLS
Beamline	X25
Temperature [K]	108
Detector technology	IMAGE PLATE
Collection date	1997-09-01
Detector	RIGAKU RAXIS
Spacegroup name	P 31 2 1
Unit cell lengths	78.050, 78.050, 142.790
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 3.000
R-factor	0.2601
Rwork	0.260
R-free	0.30800
RMSD bond length	0.011
RMSD bond angle	1.450 *
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	CNS (0.5)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	3.160
High resolution limit [Å]	3.000	3.000
Rmerge	0.094	0.410
Total number of observations	108811 *
Number of reflections	10352 *
<I/σ(I)>	4.9
Completeness [%]	98.4	94.3
Redundancy	4.8	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	6.2 *	20 *	Chen, S., (2001) J.Mol.Biol., 314, 63. *

Crystallization Reagents

ID	crystal ID	solution ID	reagent name	concentration	details
1	1	1	1,4-DIOXANE
2	1	1	MES
3	1	1	NACL
4	1	1	MGCL2
5	1	1	CAMP
6	1	1	PEG 8000
7	1	2	PEG 8000

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	CAP	0.1-0.2 (mM)
2	1	drop	protein	0.12-0.24 (mM)
3	1	drop	cAMP	2 (mM)
4	1	drop	MES	100 (mM)	pH6.2
5	1	drop		200 (mM)
6	1	drop		50 (mM)
7	1	drop	PEG8000	5-6 (%(w/v))
8	1	drop	dioxane	18-19 (%(v/v))